Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54741

- AFSK_STRCO

UniProt

P54741 - AFSK_STRCO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase AfsK

Gene

afsK

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the regulation of secondary metabolism by phosphorylating, on both Ser and Thr, the AfsR global regulatory protein involved in the control of secondary metabolism.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441ATPPROSITE-ProRule annotation
Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 5998.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase AfsK (EC:2.7.11.1)
Gene namesi
Name:afsK
Ordered Locus Names:SCO4423
ORF Names:SC6F11.21, SCD6.01
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441K → A: No autophosphorylation. Binds KbpA. 1 Publication
Mutagenesisi71 – 711S → A: No autophosphorylation. 1 Publication
Mutagenesisi128 – 1281S → A: No change in autophosphorylation. 1 Publication
Mutagenesisi168 – 1681T → A: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Very little constitutive kinase activity. 1 Publication
Mutagenesisi168 – 1681T → D: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Constitutive kinase activity. 1 Publication
Mutagenesisi168 – 1681T → E: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Some constitutive kinase activity. 1 Publication
Mutagenesisi170 – 1701T → D: No change in autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 799799Serine/threonine-protein kinase AfsKPRO_0000171234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711Phosphoserine; by autocatalysis1 Publication
Modified residuei168 – 1681Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylated mainly on threonine residues. Some phosphorylation on serine residues. Autophosphorylation on Thr-168 is the major site enhancing kinase activity towards AfsR, and is regulated though interaction with KbpA.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP54741.

PTM databases

PhosSiteiP1007968.

Interactioni

Subunit structurei

Interacts (via the N-terminal kinase domain) with KbpA; the interaction prevents autophosphorylation of AfsK.1 Publication

Protein-protein interaction databases

STRINGi100226.SCO4423.

Structurei

3D structure databases

ProteinModelPortaliP54741.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 271256Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi317 – 428112Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000033839.
InParanoidiP54741.
OMAiRFRMSND.
OrthoDBiEOG6Z0Q5X.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR002372. PQQ_repeat.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF01011. PQQ. 3 hits.
[Graphical view]
SMARTiSM00564. PQQ. 9 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54741-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL
60 70 80 90 100
AEDQLFRVRF TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL
110 120 130 140 150
EEIVNECGPM PAQAVRWLAA GVAEALQSIH GAGLVHRDLK PSNVLVVEDG
160 170 180 190 200
PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM SPEQAKDSRS VTGASDVFSL
210 220 230 240 250
GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL RPLIESCMQM
260 270 280 290 300
EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP
310 320 330 340 350
AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP
360 370 380 390 400
APVGAPDGGP VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP
410 420 430 440 450
RPGVNGADPA VPAPAPAPPE ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV
460 470 480 490 500
TSFEVHALDV ATGRRRFKTR DVAWSMAVAD GRIHASDGPT LFALDAREGA
510 520 530 540 550
DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK LWEVTGAQTD
560 570 580 590 600
FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV
610 620 630 640 650
RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV
660 670 680 690 700
TGGGVYLADY LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS
710 720 730 740 750
GKGLYTLDAV TGTPKWRFQA GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD
760 770 780 790
DGRLRWKLAT GGEITGSPVV RDGIVYACSK DRCVYALDAE KGTGTARTT
Length:799
Mass (Da):83,788
Last modified:August 14, 2001 - v2
Checksum:i4BE9BED4169F6F5B
GO

Mass spectrometryi

Molecular mass is 1638.8 Da from positions 68 - 93. Determined by ESI. 1 Publication
Molecular mass is 1718.8 Da from positions 68 - 93. Determined by ESI. Monophosphorylated.1 Publication
Molecular mass is 2236.5 Da from positions 117 - 137. Determined by ESI. 1 Publication
Molecular mass is 2109.4 Da from positions 167 - 186. Determined by ESI. 1 Publication
Molecular mass is 2189.4 Da from positions 167 - 186. Determined by ESI. Monophosphorylated.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45382 Genomic DNA. Translation: BAA08229.2.
AL939120 Genomic DNA. Translation: CAD55483.1.
RefSeqiNP_733637.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAD55483; CAD55483; CAD55483.
GeneIDi1099863.
KEGGisco:SCO4423.
PATRICi23738656. VBIStrCoe124346_4492.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45382 Genomic DNA. Translation: BAA08229.2 .
AL939120 Genomic DNA. Translation: CAD55483.1 .
RefSeqi NP_733637.1. NC_003888.3.

3D structure databases

ProteinModelPortali P54741.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO4423.

PTM databases

PhosSitei P1007968.

Proteomic databases

PRIDEi P54741.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD55483 ; CAD55483 ; CAD55483 .
GeneIDi 1099863.
KEGGi sco:SCO4423.
PATRICi 23738656. VBIStrCoe124346_4492.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000033839.
InParanoidi P54741.
OMAi RFRMSND.
OrthoDBi EOG6Z0Q5X.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 5998.

Family and domain databases

Gene3Di 2.140.10.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR002372. PQQ_repeat.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF01011. PQQ. 3 hits.
[Graphical view ]
SMARTi SM00564. PQQ. 9 hits.
[Graphical view ]
SUPFAMi SSF50998. SSF50998. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase."
    Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.
    Gene 146:47-56(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  2. "The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2)."
    Ueda K., Umeyama T., Beppu T., Horinouchi S.
    Gene 169:91-95(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  3. Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 239-240.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  5. "Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein."
    Umeyama T., Horinouchi S.
    J. Bacteriol. 183:5506-5512(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-44.
  6. "Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168."
    Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M., Ohnishi Y., Horinouchi S.
    J. Antibiot. 59:117-123(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170.

Entry informationi

Entry nameiAFSK_STRCO
AccessioniPrimary (citable) accession number: P54741
Secondary accession number(s): Q9F365, Q9L002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3